• Journal of Microbiology and Biotechnology
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• v.16 no.6
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• pp.974-978
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• 2006

The cytochrome P450 monooxygenase from the pikromycin biosynthetic gene cluster in Streptomyces venezuelae, known as PikC, was observed to hydroxylate the unnatural substrate indole to indigo. Furthermore, the site-directed mutagenesis of PikC monooxygenase led to the mutant enzyme F171Q, in which Phe171 was altered to Gln, with enhanced activity for the hydroxylation of indole. From enzyme kinetic studies, F171Q showed an approximately five-fold higher catalytic efficiency compared with the wild-type PikC. Therefore, these results demonstrate the promising application of P450s originating from Streptomyces, normally involved in polyketide biosynthesis, to generate a diverse array of other industrially useful compounds.

• The Korean Journal of Physiology and Pharmacology
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• v.1 no.5
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• pp.591-595
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• 1997

An ex vivo assay determining the flavin-containing monooxygenase (FMO) activity in perfused rat liver has been developed by assessing the rate of thiobenzamide S-oxide (TBSO) formation from the infused thiobenzamide (TB). The hepatotoxicity by TB or TBSO was not a critical factor for maintaining the FMO activity for up to 50 min. The FMO activity expressed in nmoles TBSO produced/g liver/min was the same for the recycling and non-recycling perfusion. This implies that reduction of the oxidized TBSO back to the parent compound (TB) is negligible. Hydrolysis of the collected perfusates with either ${\beta}-glucuronidase$ or arylsulfatase did not increase the TBSO level and thus, TBSO does not appear to undergo conjugation either to glucuronide or sulfate esters. Thus, measuring the rate of TB S-oxidation in the isolated perfused liver with 1 mM TB for 50 min provides a useful tool for evaluation of the hepatic FMO activity in the absence of hepatic necrosis and without the interferences caused by further conjugation or back reduction of the TBSO to the parent TB.

• Journal of Marine Bioscience and Biotechnology
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• v.10 no.2
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• pp.44-52
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• 2018

A synthetic pathway, which consisted of fatty acid double bond hydratase, alcohol dehydrogenase, and Baeyer-Villiger monooxygenase, was applied to Chlorella oil to produce ester fatty acids, which can be hydrolyzed into medium chain fatty acids. Since linoleic acid is a major fatty acid constituent of Chlorella oil, a fatty acid double bond hydratase from Lactobacillus acidophilus NBRC13951, which is able to convert linoleic acid into 13-hydroxyoctadec-9-enoic acid, was used. Recombinant Escherichia coli expressing the fatty acid double bond hydratase from L. acidophilus NBRC13951 successfully transformed linoleic acid in Chlorella oil hydrolysates into 13-hydroxyoctadec-9-enoic acid with approximately 60% conversion yield. 13-Hydroxyoctadec-9-enoic acid was further converted into ester fatty acids by the recombinant E. coli expressing a long chain secondary alcohol dehydrogenase and a Baeyer-Villiger monooxygenase. The resulting ester fatty acids were then hydrolyzed into medium chain fatty acids by a lipase. Overall, industrially relevant medium chain fatty acids were produced from Chlorella oil hydrolysates. Thereby, this study may contribute to biosynthesis of medium chain fatty acids from microalgae oils as well as long chain fatty acids.

• Journal of Microbiology
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• v.40 no.4
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• pp.249-253
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• 2002

No Abstract. See Full Text

• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.541-544
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• 2001

One of the most promising TCE treatment systems is trickling biofilter (TBF), in which monooxygenase, the corresponding enzyme for initiating growth substrate oxidation, fortuitously transforms TCE via cometabolism. TCE. however. is not easily treated by simple cometabolic biotransformation. This is mainly due to the toxicity of TCE to microbial cell and monooxygenase. In this study, we cleveloped and operated a two-stage CSTR/TBF system for the long-term continuous treatment of TCE. In the two-stage biotransfon11ation system, CSTR with cell recycle from TBR was coupled to the TBR for the reactivation of the cells deactivated during TCE degradation.

• Proceedings of the Korean Society of Soil and Groundwater Environment Conference
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• 2004.04a
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• pp.147-152
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• 2004

Aerobic cometabolism of cis-1,2-dichloroethylene (c-DCE) and c-DCE epoxide by a butane-grown mixed culture was evaluated. Transformation of c-DCE resulted in the concomitant generation of c-DCE epoxide. Chloride release studies showed nearly complete oxidative dechlorination of c-DCE (approximately 75%). Mass spectrometry confirmed tile presence of a compound with mass-to-charge-fragment ratios of 112, 83, 48, and 35. The values are in agreement with the spectra of a chemically synthesized c-DCE epoxide. Some evidences indicating the involvement of the monooxygenase in the transformation of c-DCE epoxide are: 1) $O_2$ requirement for c-DCE transformation and butane degradation; 2) butane inhibition on c-DCE transformation and vice versa; 3) the inactivation of c-DCE and c-DCE epoxide transformations by acetylene (a known monooxygenase inactivator); and 4) tire inhibition of c-DCE epoxide transformation by c-DCE.

• Proceedings of the Zoological Society Korea Conference
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• 2001.10a
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• pp.244.2-244
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• 2001

No Abstract, See Full Text

• Fisheries and Aquatic Sciences
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• v.16 no.4
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• pp.261-265
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• 2013

The study was conducted to investigate the responses of the hepatic microsomal cytochrome P450 monooxygenase system in the rock bream Oplegnathus fasciatus after chronic exposure to 0, 1, 2, 4, and $8{\mu}g/L$ tributyltin (TBT) concentrations for 4 weeks. Hepatic cytochrome 450 content and ethoxyresorufin O-deethylation (EROD) activity were found to significantly increase in fish treated with the higher concentration of TBT (${\geq}4{\mu}g/L$); however, no significant changes were observed in penthoxyresorufin O-deethylation (PROD) activity in all treated groups compared to the control group. These findings suggest that exposure to a low TBT concentration (${\geq}4{\mu}g/L$) has the potential to induce cytochrome 450 content and EROD enzyme activity in hepatic tissue in the rock bream.

• Prospectives of Industrial Chemistry
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• v.19 no.2
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• pp.28-35
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• 2016

천연가스, 셰일가스 및 바이오가스의 주성분인 메탄은 지구온난화 가스로, 감축대상인 동시에 차세대 탄소 자원으로 주목을 받고 있다. 기존의 화학적 메탄전환방법은 대규모 설비투자가 요구되는 규모의 경제가 적용되어 소규모 한계 가스전에는 활용이 어렵다. 이러한 문제점을 극복하기 위하여 최근에 생물학적 전환법이 대안으로 고려되고 있다. 메탄자화균은 메탄산화효소(methane monooxygenase)를 이용하여 상온 상압에서 메탄을 탄소원으로 사용하여 생장할 수 있다. 따라서 메탄자화균의 메탄 대사경로를 기반으로 대사공학을 활용하면 메탄으로부터의 다양한 종류의 고부가가치 산물 생산이 가능하다. 본고에서는 메탄자화균을 이용한 메탄의 바이오전환 기술의 현황 및 전망에 대하여 논의하였다.

• 한국생물공학회:학술대회논문집
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• 2005.04a
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• pp.313-313
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• 2005